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Dr. Gustav Oberdorfer, Dr. Georg Steinkellner, Dr. Clemens Stueckler, Prof. Kurt Faber and Prof. Karl Gruber Stereopreferences of Old Yellow Enzymes: Structure Correlations and Sequence Patterns in Enoate Reductases ChemCatChem 3

Version of Record online: 18 AUG 2011 | DOI: 10.1002/cctc.201100141

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From active sites and stereospecificity: Active-site structures of old yellow enzymes (OYEs) are correlated with their stereopreferences in the reduction of an aromatic nitroalkene, which leads to the identification of distinct clusters. These structural clusters are mapped onto sequence space, which yields four characteristic sequence motifs that may be used to cluster OYEs on the basis of their primary structure, as well as to predict their structural and biocatalytic properties.

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